Anti-Golgi Complex Autoantibodies in Patients with Primary Sjögren's Syndrome

Blaschek, M; Pennec, Y; Simitzis, A. M.; Goff, P. Le; Lamour, A.; Kerdraon, G.; Jouquan, Jean; Youinou, Pierre

doi:10.3109/03009748809098799

Cited by 44 publications

(29 citation statements)

References 17 publications

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“…SLE, Sjögren's syndrome) (7,(41)(42)(43)(44)(45)(46)(47), idiopathic cerebellar ataxia (48), paraneoplastic cerebellar degeneration (49), and viral infections including the Epstein-Barr virus (50) and the human immunodeficiency virus (51). In this study, we have used the antibodies from a patient with Sjögren's syndrome, a disease characterized by lymphocytic infiltrates and fibrosis of exocrine glands, to clone and characterize a unique Golgi au- toantigen.…”

Section: Isolation and Characterization Of Cdnas Encodingmentioning

confidence: 99%

Molecular Characterization of Golgin-245, a Novel Golgi Complex Protein Containing a Granin Signature

Fritzler

Lung

Hamel

et al. 1995

Journal of Biological Chemistry

100

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The serum from a Sjö gren's syndrome patient with anti-Golgi antibodies was used as a probe to isolate a 4.6-kilobase pair cDNA insert from a HeLa cDNA library. Expression of the cDNA in Escherichia coli and the in vitro translation products of the cDNA yielded a recombinant protein that migrated in SDS-polyacrylamide gel electrophoresis at 180 kDa. This protein was immunoprecipitated by the human anti-Golgi serum and by immune rabbit serum but not by normal human serum or preimmune rabbit serum. Western blot analysis showed that the prototype human and immune rabbit sera recognized a 245-kDa protein, suggesting that the isolated clone contained a partial cDNA. The 5-upstream sequence obtained by the rapid amplification of cDNA ends methodology using human placental cDNA and the combined HeLa cDNA contained 6965 base pairs and encoded a protein of 245 kDa and, like other Golgi autoantigens described earlier, is highly rich in coiledcoils. The deduced amino acid sequence included the decapeptide ESLALEELEL, which was identified as one of two signature sequences previously reported in a family of peptide hormones and neuropeptides known as "granins." This is the first report of a Golgi complex autoantigen that bears structural similarities to the granin family of proteins.

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Section: Isolation and Characterization Of Cdnas Encodingmentioning

confidence: 99%

Molecular Characterization of Golgin-245, a Novel Golgi Complex Protein Containing a Granin Signature

Fritzler

Lung

Hamel

et al. 1995

Journal of Biological Chemistry

100

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“…All of the previously reported cases had established CTDs: SLE, SS and polymyositis (PM) (1,3), SLE and RA (5), and RA and PM (13).…”

Section: Introductionmentioning

confidence: 99%

Coexistence of Autoantibodies against the Golgi Complex and Ro52 Antigen in a Patient with Nonspecific Interstitial Pneumonia

et al. 2016

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Nonspecific interstitial pneumonia (NSIP) is often associated with connective tissue diseases (CTD). The diagnosis of NSIP was confirmed in a 63-year-old man by high-resolution computed tomography and an open lung biopsy. Anti-Golgi complex autoantibodies (AGA) and anti-Ro52 antibodies were simultaneously detected at high concentrations. Autoantibodies to aminoacyl-tRNA synthetases (ARS) were negative. The patient was treated with corticosteroids for six months. During the seven-year follow-up, NSIP had a slow progression and patient had not developed the clinical features of CTD. The present study potentially demonstrates that the autoimmune process elicited by AGA and/or Ro/SSA may play a role in promoting idiopathic NSIP independently of the typical ARS routes, which has not been reported thus far.

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“…For example, naturally occurring autoantibodies have been used to identify and clone chromatin, nucleolar, nuclear envelope, and cytoplasmic proteins (reviewed in references 1-3). Antibodies directed against the Golgi complex have been reported in the sera of patients with SLE (4), Sj6gren's syndrome and other systemic rheumatic diseases (4)(5)(6)(7)(8)(9), idiopathic cerebellar ataxia (10), paraneoplastic cerebellar degeneration (11), and viral infections, including the EBV (12), and HIV (13). This study reports the identification and cloning of two Golgi autoantigens that react with autoantibodies in the sera of patients with autoimmune diseases.…”

mentioning

confidence: 99%

Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex.

Fritzler

Hamel

Ochs

et al. 1993

The Journal of Experimental Medicine

134

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Sllmmal~Serum autoantibodies from a patient with autoantibodies directed against the Golgi complex were used to screen clones from a HepG2 XZ_ap cDNA library. Three related clones, designated SY2, SY10, and SYll, encoding two distinct polypeptides were purified for further analysis. Antibodies affinity purified by adsorption to the XZ_ap-cloned recombinant proteins and antibodies from NZW rabbits immunized with purified recombinant proteins reproduced Golgi staining and bound two different proteins, 95 and 160 kD, from whole cell extracts. The SYll protein was provisionally named golgin-95 and the SY2/SY10 protein was named golgin-160. The deduced amino acid sequence of the cDNA clone of SY2 and SYll represented 58.7-and 70-kD proteins of 568 and 620 amino acids. The in vitro translation products of SY2 and SYll cDNAs migrated in SDS-PAGE at 65 and 95 kD, respectively. The in vitro translated proteins were immunoprecipitated by human anti-Golgi serum or immune rabbit serum, but not by normal human serum or preimmune rabbit serum. Features of the cDNA suggested that SY11 was a full-length clone encoding golgin-95 but SY2 and SY10 together encoded a partial sequence of golgin-160. Analysis of the SY11 recombinant protein identified a leucine zipper spanning positions 419-455, a glutamic acid-rich tract spanning positions 322-333, and a proline-rich tract spanning positions 67-73. A search of the SwissProt data bank indicated sequence similarity of SYll to human restin, the heavy chain of kinesin, and the heavy chain of myosin. SY2 shared sequence similarity with the heavy chain of myosin, the USO1 transport protein from yeast, and the 150-kD cytoplasmic dynein-associated polypeptide. Sequence analysis demonstrated that golgin-95 and golgin-160 share 43% sequence similarity and, therefore, may be functionally related proteins.

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Anti-Golgi Complex Autoantibodies in Patients with Primary Sjögren's Syndrome

Cited by 44 publications

References 17 publications

Molecular Characterization of Golgin-245, a Novel Golgi Complex Protein Containing a Granin Signature

Molecular Characterization of Golgin-245, a Novel Golgi Complex Protein Containing a Granin Signature

Coexistence of Autoantibodies against the Golgi Complex and Ro52 Antigen in a Patient with Nonspecific Interstitial Pneumonia

Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex.

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